4bj8: Difference between revisions
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== | ==Zebavidin== | ||
[[4bj8]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BJ8 OCA]. | <StructureSection load='4bj8' size='340' side='right'caption='[[4bj8]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bj8]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BJ8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bj8 OCA], [https://pdbe.org/4bj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bj8 RCSB], [https://www.ebi.ac.uk/pdbsum/4bj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bj8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E7F650_DANRE E7F650_DANRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The avidin protein family members are well known for their high affinity towards D-biotin and high structural stability. These properties make avidins valuable tools for a wide range of biotechnology applications. We have identified a new member of the avidin family in the zebrafish (Danio rerio) genome, hereafter called zebavidin. The protein is highly expressed in the gonads of both male and female zebrafish and in the gills of male fish, but our data suggest that zebavidin is not crucial for the developing embryo. Biophysical and structural characterisation of zebavidin revealed distinct properties not found in any previously characterised avidins. Gel filtration chromatography and native mass spectrometry suggest that the protein forms dimers in the absence of biotin at low ionic strength, but assembles into tetramers upon binding biotin. Ligand binding was analysed using radioactive and fluorescently labelled biotin and isothermal titration calorimetry. Moreover, the crystal structure of zebavidin in complex with biotin was solved at 2.4 A resolution and unveiled unique ligand binding and subunit interface architectures; the atomic-level details support our physicochemical observations. | |||
Zebavidin - an avidin-like protein from zebrafish.,Taskinen B, Zmurko J, Ojanen M, Kukkurainen S, Parthiban M, Maatta JA, Leppiniemi J, Janis J, Parikka M, Turpeinen H, Ramet M, Pesu M, Johnson MS, Kulomaa MS, Airenne TT, Hytonen VP PLoS One. 2013 Oct 24;8(10):e77207. doi: 10.1371/journal.pone.0077207. PMID:24204770<ref>PMID:24204770</ref> | |||
<ref | |||
[[Category: Airenne | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: Hytonen | </div> | ||
[[Category: Johnson | <div class="pdbe-citations 4bj8" style="background-color:#fffaf0;"></div> | ||
[[Category: Kulomaa | |||
[[Category: Niederhauser | ==See Also== | ||
[[Category: Parthiban | *[[Avidin 3D structures|Avidin 3D structures]] | ||
[[Category: Zmurko | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Danio rerio]] | |||
[[Category: Large Structures]] | |||
[[Category: Airenne TT]] | |||
[[Category: Hytonen VP]] | |||
[[Category: Johnson MS]] | |||
[[Category: Kulomaa MS]] | |||
[[Category: Niederhauser B]] | |||
[[Category: Parthiban M]] | |||
[[Category: Zmurko J]] | |||
Latest revision as of 14:52, 20 December 2023
ZebavidinZebavidin
Structural highlights
FunctionPublication Abstract from PubMedThe avidin protein family members are well known for their high affinity towards D-biotin and high structural stability. These properties make avidins valuable tools for a wide range of biotechnology applications. We have identified a new member of the avidin family in the zebrafish (Danio rerio) genome, hereafter called zebavidin. The protein is highly expressed in the gonads of both male and female zebrafish and in the gills of male fish, but our data suggest that zebavidin is not crucial for the developing embryo. Biophysical and structural characterisation of zebavidin revealed distinct properties not found in any previously characterised avidins. Gel filtration chromatography and native mass spectrometry suggest that the protein forms dimers in the absence of biotin at low ionic strength, but assembles into tetramers upon binding biotin. Ligand binding was analysed using radioactive and fluorescently labelled biotin and isothermal titration calorimetry. Moreover, the crystal structure of zebavidin in complex with biotin was solved at 2.4 A resolution and unveiled unique ligand binding and subunit interface architectures; the atomic-level details support our physicochemical observations. Zebavidin - an avidin-like protein from zebrafish.,Taskinen B, Zmurko J, Ojanen M, Kukkurainen S, Parthiban M, Maatta JA, Leppiniemi J, Janis J, Parikka M, Turpeinen H, Ramet M, Pesu M, Johnson MS, Kulomaa MS, Airenne TT, Hytonen VP PLoS One. 2013 Oct 24;8(10):e77207. doi: 10.1371/journal.pone.0077207. PMID:24204770[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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